EC |
2.3.3.8 |
Accepted name: |
ATP citrate synthase |
Reaction: |
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA |
Other name(s): |
ATP-citric lyase; ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-→acetyl-CoA] (ATP-dephosphorylating); acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating); adenosine triphosphate citrate lyase; citrate cleavage enzyme; citrate-ATP lyase; citric cleavage enzyme; ATP citrate (pro-S)-lyase |
Systematic name: |
acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating] |
Comments: |
The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate—CoA ligase). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-95-6 |
References: |
1. |
Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502] |
2. |
Srere, P.A. and Lipmann, F. An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A. J. Am. Chem. Soc. 75 (1953) 4874. |
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[EC 2.3.3.8 created 1965 as EC 4.1.3.8, modified 1986, transferred 2002 to EC 2.3.3.8] |
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EC |
2.8.3.10 |
Accepted name: |
citrate CoA-transferase |
Reaction: |
acetyl-CoA + citrate = acetate + (3S)-citryl-CoA |
Systematic name: |
acetyl-CoA:citrate CoA-transferase |
Comments: |
The enzyme is a component of EC 4.1.3.6 [citrate (pro-3S)-lyase]. Also catalyses the transfer of thioacyl carrier protein from its acetyl thioester to citrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65187-14-6 |
References: |
1. |
Dimroth, P., Loyal, R. and Eggerer, H. Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate. Eur. J. Biochem. 80 (1977) 479–488. [DOI] [PMID: 336371] |
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[EC 2.8.3.10 created 1984] |
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EC |
3.1.2.7 |
Accepted name: |
glutathione thiolesterase |
Reaction: |
S-acylglutathione + H2O = glutathione + a carboxylate |
Other name(s): |
citryl-glutathione thioesterhydrolase |
Systematic name: |
S-acylglutathione hydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-99-4 |
References: |
1. |
Kielley, W.W. and Bradley, L.B. Glutathione thiolesterase. J. Biol. Chem. 206 (1954) 327–338. [PMID: 13130552] |
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[EC 3.1.2.7 created 1961] |
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EC |
3.5.1.68 |
Accepted name: |
N-formylglutamate deformylase |
Reaction: |
N-formyl-L-glutamate + H2O = formate + L-glutamate |
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For diagram of histidine catabolism, click here |
Other name(s): |
β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme |
Systematic name: |
N-formyl-L-glutamate amidohydrolase |
Comments: |
The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97286-12-9 |
References: |
1. |
Hu, L., Mulfinger, L.M. and Phillips, A.T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J. Bacteriol. 169 (1987) 4696–4702. [DOI] [PMID: 3308850] |
2. |
Miyake, M., Innami, T. and Kakimoto, Y. A β-citryl-L-glutamate-hydrolysing enzyme in rat testes. Biochim. Biophys. Acta 760 (1983) 206–214. [DOI] [PMID: 6414521] |
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[EC 3.5.1.68 created 1989] |
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EC |
4.1.3.6 |
Accepted name: |
citrate (pro-3S)-lyase |
Reaction: |
citrate = acetate + oxaloacetate |
Other name(s): |
citrase; citratase; citritase; citridesmolase; citrate aldolase; citric aldolase; citrate lyase; citrate oxaloacetate-lyase; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-→acetate] |
Systematic name: |
citrate oxaloacetate-lyase (forming acetate from the pro-S carboxymethyl group of citrate) |
Comments: |
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.10 (citrate CoA-transferase) and EC 4.1.3.34 (citryl-CoA lyase). EC 3.1.2.16, citrate lyase deacetylase, deacetylates and inactivates the enzyme. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-83-3 |
References: |
1. |
Dagley, S. and Dawes, E.A. Citridesmolase: its properties and mode of action. Biochim. Biophys. Acta 17 (1955) 177–184. [DOI] [PMID: 13239657] |
2. |
Dimroth, P., Loyal, R. and Eggerer, H. Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate. Eur. J. Biochem. 80 (1977) 479–488. [DOI] [PMID: 336371] |
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[EC 4.1.3.6 created 1961] |
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EC |
4.1.3.34 |
Accepted name: |
citryl-CoA lyase |
Reaction: |
(3S)-citryl-CoA = acetyl-CoA + oxaloacetate |
Other name(s): |
(3S)-citryl-CoA oxaloacetate-lyase |
Systematic name: |
(3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming) |
Comments: |
The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 131095-35-7 |
References: |
1. |
Dimroth, P., Loyal, R. and Eggerer, H. Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate. Eur. J. Biochem. 80 (1977) 479–488. [DOI] [PMID: 336371] |
2. |
Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502] |
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[EC 4.1.3.34 created 1984, modified 1986] |
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EC |
6.2.1.18 |
Accepted name: |
citrate—CoA ligase |
Reaction: |
ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA |
Glossary: |
citrate = 2-hydroxypropane-1,2,3-tricarboxylate |
Other name(s): |
citryl-CoA synthetase; citrate:CoA ligase; citrate thiokinase |
Systematic name: |
citrate:CoA ligase (ADP-forming) |
Comments: |
The enzyme is a component of EC 2.3.3.8 ATP citrate synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 856428-87-0 |
References: |
1. |
Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502] |
2. |
Aoshima, M., Ishii, M. and Igarashi, Y. A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 52 (2004) 751–761. [DOI] [PMID: 15101981] |
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[EC 6.2.1.18 created 1986] |
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EC |
6.3.1.17 |
Accepted name: |
β-citrylglutamate synthase |
Reaction: |
ATP + citrate + L-glutamate = ADP + phosphate + β-citryl-L-glutamate |
Other name(s): |
NAAG synthetase I; NAAGS-I; RIMKLB (gene name) (ambiguous) |
Systematic name: |
citrate:L-glutamate ligase (ADP-forming) |
Comments: |
The enzyme, found in animals, also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Collard, F., Stroobant, V., Lamosa, P., Kapanda, C.N., Lambert, D.M., Muccioli, G.G., Poupaert, J.H., Opperdoes, F. and Van Schaftingen, E. Molecular identification of N-acetylaspartylglutamate synthase and β-citrylglutamate synthase. J. Biol. Chem. 285 (2010) 29826–29833. [DOI] [PMID: 20657015] |
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[EC 6.3.1.17 created 2014] |
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EC
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6.3.2.27
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Deleted entry: | The activity is covered by two independent enzymes, EC 6.3.2.38 N2-citryl-N6-acetyl-N6-hydroxylysine synthase, and EC 6.3.2.39, aerobactin synthase |
[EC 6.3.2.27 created 2002, modified 2006, deleted 2012] |
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EC |
6.3.2.38 |
Accepted name: |
N2-citryl-N6-acetyl-N6-hydroxylysine synthase |
Reaction: |
2 ATP + citrate + N6-acetyl-N6-hydroxy-L-lysine + H2O = 2 ADP + 2 phosphate + N6-acetyl-N2-citryl-N6-hydroxy-L-lysine |
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For diagram of aerobactin biosynthesis, click here |
Glossary: |
citryl = 3-hydroxy-3,4-dicarboxybutanoyl |
Other name(s): |
Nα-citryl-Nε-acetyl-Nε-hydroxylysine synthase; iucA (gene name) |
Systematic name: |
citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (AMP-forming) |
Comments: |
Requires Mg2+. The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme is believed to form an adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175–184. [DOI] [PMID: 4313071] |
2. |
Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096–3101. |
3. |
de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523] |
4. |
Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437–443. |
5. |
Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis
independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601–611. [DOI] [PMID: 15719346] |
6. |
Oves-Costales, D., Kadi, N. and Challis, G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) (2009) 6530–6541. [PMID: 19865642] |
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[EC 6.3.2.38 created 2012, modified 2019] |
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EC |
6.3.2.39 |
Accepted name: |
aerobactin synthase |
Reaction: |
ATP + N2-citryl-N6-acetyl-N6-hydroxy-L-lysine + N6-acetyl-N6-hydroxy-L-lysine = AMP + diphosphate + aerobactin |
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For diagram of aerobactin biosynthesis, click here |
Other name(s): |
iucC (gene name) |
Systematic name: |
N2-citryl-N6-acetyl-N6-hydroxy-L-lysine:N6-acetyl-N6-hydroxy-L-lysine ligase (AMP-forming) |
Comments: |
Requires Mg2+. The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore. It belongs to a class of siderophore synthases known as type C nonribosomal peptide synthase-independent synthases (NIS). Type C enzymes are responsible for the formation of amide or ester bonds between a variety of substrates and a prochiral carboxyl group of a citrate molecule that is already linked to a different moiety at its other prochiral carboxyl group. The enzyme is believed to form an adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175–184. [DOI] [PMID: 4313071] |
2. |
Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096–3101. |
3. |
Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437–443. |
4. |
de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523] |
5. |
de Lorenzo, V. and Neilands, J.B. Characterization of iucA and iucC genes of the aerobactin system of plasmid ColV-K30 in Escherichia coli. J. Bacteriol. 167 (1986) 350–355. [DOI] [PMID: 3087960] |
6. |
Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis
independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601–611. [DOI] [PMID: 15719346] |
7. |
Oves-Costales, D., Kadi, N. and Challis, G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) (2009) 6530–6541. [PMID: 19865642] |
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[EC 6.3.2.39 created 2012, modified 2019] |
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EC |
6.3.2.41 |
Accepted name: |
N-acetylaspartylglutamate synthase |
Reaction: |
ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate |
Other name(s): |
N-acetylaspartylglutamate synthetase; NAAG synthetase; NAAGS; RIMKLA (gene name) (ambiguous); RIMKLB (gene name) (ambiguous) |
Systematic name: |
N-acetyl-L-aspartate:L-glutamate ligase (ADP, N-acetyl-L-aspartyl-L-glutamate-forming) |
Comments: |
The enzyme, found in animals, produces the neurotransmitter N-acetyl-L-aspartyl-L-glutamate. One isoform also has the activity of EC 6.3.1.17, β-citrylglutamate synthase [2], while another isoform has the activity of EC 6.3.2.42, N-acetylaspartylglutamylglutamate synthase [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Becker, I., Lodder, J., Gieselmann, V. and Eckhardt, M. Molecular characterization of N-acetylaspartylglutamate synthetase. J. Biol. Chem. 285 (2010) 29156–29164. [DOI] [PMID: 20643647] |
2. |
Collard, F., Stroobant, V., Lamosa, P., Kapanda, C.N., Lambert, D.M., Muccioli, G.G., Poupaert, J.H., Opperdoes, F. and Van Schaftingen, E. Molecular identification of N-acetylaspartylglutamate synthase and β-citrylglutamate synthase. J. Biol. Chem. 285 (2010) 29826–29833. [DOI] [PMID: 20657015] |
3. |
Lodder-Gadaczek, J., Becker, I., Gieselmann, V., Wang-Eckhardt, L. and Eckhardt, M. N-acetylaspartylglutamate synthetase II synthesizes N-acetylaspartylglutamylglutamate. J. Biol. Chem. 286 (2011) 16693–16706. [DOI] [PMID: 21454531] |
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[EC 6.3.2.41 created 2014] |
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EC |
6.3.2.57 |
Accepted name: |
staphyloferrin A synthase |
Reaction: |
ATP + N5-[(S)-citryl]-D-ornithine + citrate = AMP + diphosphate + staphyloferrin A |
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For diagram of staphyloferrin A biosynthesis, click here |
Glossary: |
staphyloferrin A = N2-[(R)-citryl],N5-[(S)-citryl]-D-ornithine
citryl = 3-hydroxy-3,4-dicarboxybutanoyl |
Other name(s): |
sfnaB (gene name) |
Systematic name: |
N5-[(S)-citryl]-D-ornithine:citrate ligase (staphyloferrin A-forming) |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last step in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cotton, J.L., Tao, J. and Balibar, C.J. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48 (2009) 1025–1035. [PMID: 19138128] |
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[EC 6.3.2.57 created 2019] |
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EC |
6.3.2.58 |
Accepted name: |
D-ornithine—citrate ligase |
Reaction: |
ATP + D-ornithine + citrate = AMP + diphosphate + N5-[(S)-citryl]-D-ornithine |
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For diagram of staphyloferrin A biosynthesis, click here |
Glossary: |
staphyloferrin A = N2-[(R)-citryl],N5-[(S)-citryl]-D-ornithine |
Other name(s): |
sfnaD (gene name) |
Systematic name: |
D-ornithine:citrate ligase {3-[(2-aminopentan-5-oylcarbamoyl)methyl]-3-hydroxybutanoate-forming} |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cotton, J.L., Tao, J. and Balibar, C.J. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48 (2009) 1025–1035. [PMID: 19138128] |
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[EC 6.3.2.58 created 2019] |
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